Premium
An engineered site for protein kinase C flanking the SV40 large T‐antigen NLS confers phorbol ester‐inducible nuclear import
Author(s) -
Xiao Chong-Yun,
Jans David A
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01157-0
Subject(s) - nuclear transport , nuclear localization sequence , protein kinase c , activator (genetics) , nls , microbiology and biotechnology , nuclear protein , nuclear export signal , protein kinase a , phorbol , cell nucleus , biology , kinase , chemistry , biochemistry , nucleus , gene , transcription factor
Nuclear import of simian virus SV40 large tumour antigen (T‐ag) is enhanced by the protein kinase CK2 (CK2) site flanking the nuclear localisation sequence (NLS). We report here that replacement of this site with a consensus site for protein kinase C (PK‐C) can alter the regulation of T‐ag nuclear import and render it inducible by phorbol ester. Measurement of nuclear import kinetics using fluorescently labelled proteins and confocal laser scanning microscopy show that the introduced PK‐C site is functional in enhancing T‐ag nuclear import compared to a protein lacking the CK2 site. Treatment with the PK‐C activator phorbol 12‐myristate 13‐acetate (PMA) further increases the level of maximal nuclear accumulation and the initial nuclear import rate. This engineered PMA‐responsive NLS may have application in targeting of molecules of interest to the nucleus in response to agents stimulating PK‐C.